12524 Results for: "ENZO LIFE SCIENCES"

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The Hsp90 family of heat shock proteins represents one of the most abundantly expressed and highly conserved families of cellular chaperones whose expression can be upregulated under conditions of cellular stress, and includes cytoplasmic (Hsp90-alpha/beta), ER (grp94), and mitochondrial (TRAP1) localized members. Structurally, Hsp90 is characterized by an N-terminal ATP-binding domain, a medial substrate-binding domain, and a C-terminal dimerization motif. Hsp90 dimers function in cooperation with cochaperones (e.g. Hsp40, Hsp70, Hop, p23) to stabilize a multitude of client protein substrates, including steroid hormone receptors, protein kinases, and transcription factors. The essential binding and hydrolysis of ATP by Hsp90 is inhibited by ansamycin drugs (e.g. geldanamycin, 17-AAG) which occupy the N-terminal Hsp90 nucleotide-binding pocket. Many Hsp90 client proteins such as erbB2/Her-2, c-raf, bcr-abl, p53, and hTERT, are members of well characterized oncogenic pathways, making Hsp90 inhibitors useful anticancer agents.

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The 90 kDa molecular chaperone family includes 90 kDa heat shock protein Hsp90 and 94 kDa glucose-regulated protein grp94, both major molecular chaperones of the cytosol and the endoplasmic reticulum. Mammalian cells express inducible Hsp90 alpha and constitutive Hsp90 beta isoforms that are encoded by separate genes. The amino acid sequences of human and yeast Hsp90 alpha are 85% and 90% homologous to those of Hsp90 beta, respectively. All known members of the Hsp90 protein family are highly conserved, especially in the N-terminal and C-terminal regions containing independent chaperone sites with different substrate specificity. These ubiquitous and highly conserved proteins account for 1-2% of all cellular protein in most cells. Hsp90 functions as part of the cell's powerful network of chaperones to fight the deleterious consequences of protein unfolding caused by non-physiological conditions. In the absence of stress, however, Hsp90 provides a necessary component of such fundamental cellular processes as hormone signaling and cell cycle control by serving as a chaperone for many key signaling molecules including steroid receptors, cell cycle kinases involved in signal transduction, and p53. As many of these client proteins are known oncogenes, Hsp90 inhibitors such as 17-AAG, a geldanamycin analog, have been of benefit in the treatment of many cancers.

Supplier: ENZO LIFE SCIENCES

The Hsp90 family of heat shock proteins represents one of the most abundantly expressed and highly conserved families of cellular chaperones whose expression can be upregulated under conditions of cellular stress, and includes cytoplasmic (Hsp90-alpha/beta), ER (grp94), and mitochondrial (TRAP1) localized members. Structurally, Hsp90 is characterized by an N-terminal ATP-binding domain, a medial substrate-binding domain, and a C-terminal dimerization motif. Hsp90 dimers function in cooperation with cochaperones (e.g. Hsp40, Hsp70, Hop, p23) to stabilize a multitude of client protein substrates, including steroid hormone receptors, protein kinases, and transcription factors. The essential binding and hydrolysis of ATP by Hsp90 is inhibited by ansamycin drugs (e.g. geldanamycin, 17-AAG) which occupy the N-terminal Hsp90 nucleotide-binding pocket. Many Hsp90 client proteins such as erbB2/Her-2, c-raf, bcr-abl, p53, and hTERT, are members of well characterized oncogenic pathways, making Hsp90 inhibitors useful anticancer agents.

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eNOS activator

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NMDA receptor antagonist.

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Angiotensin I/II (1-7)

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Syntaxins are type II integral membrane proteins localized to membranes that regulate vesicle transport, protein maturation, and exocytosis. Syntaxin 1A resides in the nerve terminals of sensory neurons and nerve fibers reaching small blood vessels. Syntaxin 2 localizes to the apical plasma membrane and regulates epithelial-mesenchymal interactions. Syntaxin 6 is primarily localized to the trans-Golgi network, and partially co-localizes with AP-1 on clathrin-coated membranes. Syntaxin 13 is ubiquitously expressed and localizes to the tubular early and recycling endosomes, as well as endosomal vacuoles.

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Produced in E. coli.

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Produced in E. coli.

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Produced in E. coli. Full length human arginase I.

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Isolated from human plasma.

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Produced in insect cells.

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Produced in E. coli. Human 14-3-3η is fused at the C-terminus to a His-tag.

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Produced in E. coli. Full length human CDC25B.

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Produced in insect cells. Full length active PKCε (protein kinase C ε).

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Potent and cell permeable proteasome inhibitor. Inhibits the chymotrypsin-like activity of the 26S proteasome (MCP; multicatalytic proteinase complex). Does not inhibit the peptidylglutamyl-peptide hydrolyzing activity of the MPC.

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Caspase and granzyme substrate

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Caspase-4 substrate

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Protease inhibitor

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Host: Rabbit

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Host: Rabbit

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Host: Rabbit

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Cytochrome p450 is a highly conserved and diverse family of heme-containing proteins that function in the metabolism of numerous endogenous and exogenous substrates.

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Produced in E.coli.

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Isotype matched controls are useful in flow cytometry to determine a gross estimate of non-specific binding that may be observed with a specific antibody of interest. In general, an isotype control should be of the same species and isotype as the antibody of interest, used at the same concentration, and conjugated to the same fluorophore. This reagent is an IgG1 isotype mouse monoclonal antibody (Clone # MOPC-21), conjugated to DyLight™-488. It is intended for use as an isotype control antibody for flow cytometry.

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Heme Oxygenase-1 (HO-1) also known as Hsp32, is the inducible isoform of heme oxygenase that catalyzes the NADPH, oxygen, and cytochrome P450 reductase dependent oxidation of heme to carbon monoxide, ferrous iron and biliverdin which is rapidly reduced to bilirubin. These products of the HO reaction have important physiological effects: carbon monoxide is a potent vasodilator and has been implicated to be a physiological regulator of cGMP and vascular tone; biliverdin and its product bilirubin are potent antioxidants; "free" iron increases oxidative stress and regulates the expression of many mRNAs (e.g., DCT-1, ferritin and transferring receptor) by affecting the conformation of iron regulatory protein (IRP)-1 and its binding to iron regulatory elements (IREs) in the 5'- or 3'- UTRs of the mRNAs. To date, three identified heme oxygenase isoforms are part of the HO system that catalyze heme into biliverdin and carbon monoxide. These are inducible HO-1 or Hsp32, constitutive HO-2 that is abundant in the brain and testis, and HO-3 which is related to HO-2 but is the product of a different gene. The HO system is the rate-limiting step in heme degradation and HO activity decreases the levels of heme which is a well known potent catalyst of lipid peroxidation and oxygen radical formation.

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Blm10 (mammalian homolog PA200) is a large 246kDa regulatory protein that binds to the 20S proteasome core particle (CP). Blm10 recognizes pre-activated open gate CP which is assumed to exist in equilibrium with inactive closed gate CP. Blm10 distinguishes gate conformations, regulates CP activation, and has been shown to be involved in CP maturation.

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Host: Rabbit

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Phosphatidylinositol 3-kinase (PI3-K) is a lipid kinase that phosphorylates the inositol ring of phosphatidylinositol and related compounds at the 3

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Researchers cloned DJ-1 protein, consisting of 189 amino acids, from a HeLa cell cDNA library as a oncogene which weakly transformed NIH3T3 cells. Cotransfection with ras or c-myc enhances transformation by DJ-11. DJ-1 expression is induced by growth signals, and it is translocated from the cytoplasm to the nucleus during the S phase without the presence of any nuclear localization signals. In addition to its potential involvement in ras-mediated signal transduction pathways, DJ-1 is known to regulate transcription of androgen-responsive genes, and is sensitive to oxidative stress. DJ-1 is ubiquitously expressed in various human tissues including the brain, with high expression in astrocytes of the frontal cortex and substantia nigra. Homozygous mutations in the DJ-1 gene have been shown to cause early-onset autosomal recessive Parkinson’s disease.